ID BGALB_SCLS1 Reviewed; 1008 AA. AC A7EBU5; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Probable beta-galactosidase B; DE EC=3.2.1.23; DE AltName: Full=Lactase B; DE Flags: Precursor; GN Name=lacB; ORFNames=SS1G_02781; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) OS (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues CC in beta-D-galactosides.; EC=3.2.1.23; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH476623; EDN99923.1; -; Genomic_DNA. DR RefSeq; XP_001596561.1; XM_001596511.1. DR AlphaFoldDB; A7EBU5; -. DR SMR; A7EBU5; -. DR GlyCosmos; A7EBU5; 15 sites, No reported glycans. DR EnsemblFungi; EDN99923; EDN99923; SS1G_02781. DR GeneID; 5492844; -. DR KEGG; ssl:SS1G_02781; -. DR VEuPathDB; FungiDB:sscle_04g037140; -. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_005732_2_1_1; -. DR InParanoid; A7EBU5; -. DR OMA; GGCPGDI; -. DR OrthoDB; 1032627at2759; -. DR Proteomes; UP000001312; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005773; C:vacuole; IBA:GO_Central. DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1. DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR018954; Betagal_dom2. DR InterPro; IPR037110; Betagal_dom2_sf. DR InterPro; IPR025972; BetaGal_dom3. DR InterPro; IPR036833; BetaGal_dom3_sf. DR InterPro; IPR025300; BetaGal_jelly_roll_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR031330; Gly_Hdrlase_35_cat. DR InterPro; IPR001944; Glycoside_Hdrlase_35. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR23421:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 1. DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1. DR Pfam; PF13364; BetaGal_ABD2; 2. DR Pfam; PF10435; BetaGal_dom2; 1. DR Pfam; PF13363; BetaGal_dom3; 1. DR Pfam; PF01301; Glyco_hydro_35; 1. DR PRINTS; PR00742; GLHYDRLASE35. DR SMART; SM01029; BetaGal_dom2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1008 FT /note="Probable beta-galactosidase B" FT /id="PRO_0000395233" FT ACT_SITE 193 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 305 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT BINDING 87 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 133 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 370 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 20 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 208 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 453 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 594 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 624 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 681 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 703 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 782 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 788 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 816 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 826 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 879 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 268..321 FT /evidence="ECO:0000250" SQ SEQUENCE 1008 AA; 110685 MW; 52E5C90A03793D5E CRC64; MLLQSLFAWA LAIGPCIAQN STNSTWPIHN NGLTTQVEWD HYSLMVDGQR FFLWSGEFHY WRIPVPELWV DVLQKVKAAG FNTFAIYTHW YFHNPNPNTL DFENAAHNFT KIFDLAKELG MFVVFRPGPY VNAESNAGAF PLWLTTGAYG ALRNNDERYT EAWTPFWEKV ASIVAPYQFT NGGNVLTYQI ENELGSQWRG TPSNKVPNLS SVEYMEALEA SARAHGITIP FQANDPNLNS DSWSKDFYDG YGSVDIYGMD SYPACWTCNL TECDSTNGAY KAFNVIDYYD HFEAISPTQP SFLPEFQGGS FNPWGGPEGG CPENSPADFA NLFYRNNVGQ RVTAMSLYMI YGGTNWGWLA APVVATSYDY SSPISENRMI NDKYAETKLF GHFLRVAKDL TKTDRIGTGK TASTNPNVVY SEIRNPDTNA AFYVTIHKES TVGTREEFYI NANTSKGAFK IPQKAASIVL NGFQSKIIVT DFNFGSHSLL YSTAEVLSHS IVDDQDILAL WMPTGEAGEF VVTGAKSGSV SSCGGCSSVG FYPQGDDLLV TISQSKGISV LTFDDGLRVL VMDRSFAYEF WVPVLTADPF SPANETVFVQ GPSLVRSAAY SSDGSTLDLT GDNNGTSTQI QVFPPKSVSK VTWNGQVITT EKTDYDSLIG SLTGPALDSL TLPTISGWKA NDSLPERLPT YDDSWWVAAD HMNTSNPTKP ETLPVLYIDD YGYHVGNHLW RGRFEGSASG VYLSVTGGRA FGYSAWLNGE FIGSYLGAAY PDTGKLTLSF SNVTVNSNST NILLVLQDNS GHDETSEALN PRGINNATLI SSSTKNFTSW KVTGTAGKPD TAIDPVRGIL SEGGLYAERL GWHLPDFDDS EWSSASPSNV SSSAGVTFYR TTVSLAIPTG LDVAISFTLK ASPSNAALRV LLFVNGYQYG RFSPWIGNQV EFPVPPGILN YDGDNVIGLS VWRQEEGDES MGVNVGWKVT EAFASSFEPI FDAAYLQPGW TDERLQYA //